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KMID : 0578319910010040397
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Molecules and Cells
1991 Volume.1 No. 4 p.397 ~ p.401
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Interaction between Polyalbumin and Pre-32 Reion of Hepatitis B Surface antigen Does Not Require the Whole Native Structure of Human Serum Albumin
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Yun, Hye Young
kweon, Hye Young/Lee, Myung Kyu/Kim, Kil Lyong/Hahm, Kyung-Soo
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Abstract
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Human serum albumin was treated with glutaraldehyde and the modified products were separated by size into three species: monomer, dimer and polymer. All the species produced from native human serum albumin bound to pre-S2 region (120-174) of hepatitis B virus surface antigen. The same was true of three modified species which were derived from the denatured human serum albumin. Receptor-ligand immunoblotting of human serum albumin cleaved by cyanogen bromide and fixed by glutaraldehyde indicated that binding of pre-S2 to polyalbumin could be confined to at least three segments (amino acids 124-297, 329445 and 446-547) of human serum albumin.
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